BMRB Entry 34358

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34358
MolProbity Validation Chart

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Title:
NMR solution structure of LSR2 binding domain.
Deposition date:
2019-01-30
Original release date:
2019-10-03
Authors:
Barthe, P.; Cohen-Gonsaud, M.; Mukamolova, G.
Citation:

Citation: Alqaseer, Kawther; Turapov, Obolbek; Barthe, Philippe; Jagatia, Heena; De Visch, Angelique; Roumestand, Christian; Wegrzyn, Malgorzata; Bartek, Iona; Voskuil, Martin; O'Hare, Helen; Ajuh, Paul; Bottrill, Andrew; Witney, Adam; Cohen-Gonsaud, Martin; Waddell, Simon; Mukamolova, Galina. "Protein kinase B controls Mycobacterium tuberculosis growth via phosphorylation of the transcriptional regulator Lsr2 at threonine 112"  Mol. Microbiol. 112, 1847-1862 (2019).
PubMed: 31562654

Assembly members:

Assembly members:
entity_1, polymer, 50 residues, 5396.921 Da.

Natural source:

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 83332   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMSGSGRGRGAIDREQSAA IREWARRNGHNVSTRGRIPA DVIDAYHAAT

Data sets:
Data typeCount
15N chemical shifts53
1H chemical shifts301

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 50 residues - 5396.921 Da.

1   GLYHISMETSERGLYSERGLYARGGLYARG
2   GLYALAILEASPARGGLUGLNSERALAALA
3   ILEARGGLUTRPALAARGARGASNGLYHIS
4   ASNVALSERTHRARGGLYARGILEPROALA
5   ASPVALILEASPALATYRHISALAALATHR

Samples:

sample_1: LSR2 protein, [U-15N], 0.5 mM

sample_2: LSR2 protein, [U-15N], 0.5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 bar; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D DQF-COSYsample_2isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CINDY, Padilla - chemical shift assignment

Gifa, Delsuc - peak picking

NMR spectrometers:

  • Bruker AVANCE III 800 MHz
  • Bruker AVANCE III 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks